Mutation locating

Azidomethemoglobin the heme iron atoms are in the low-spin ferric state with one unpaired electron per heme iron Human fetal hemoglobin Mutation located in the amino-terminal region of the p chain High-affinity mutant with the mutation located in the 01 2 subunit interface Mutation located in the amino-terminal region of the p chain High-affinity mutant with the mutation located in the a,p2 subunit interface High-affinity mutant with the mutation located in the 01 2 subunit interface... 

Mutation in the distal heme pocket of the p chain the heme iron atoms in the p chains are in the high-spin ferric state, i.e., (a2p2), with five unpaired electrons per heme iron in the p chains and four unpaired electrons per heme iron in the a chains a naturally occurring valency hybrid hemoglobin Mutation located in the heme pocket of the P chain... 

High-affinity mutant with the mutation located in the a]P2 subunit interface... 

G8 Mutations Location in structure Generation Proposed role for 5-6C8 mutations... 

The overmodification of collagen from patients 1 and 2 is weak because it occurs only on the N-terminal side of the mutation. Mutations located closer to the C-terminal end lead to substantially larger overhydroxylation and overgly-cosylation. In principle, this overmodification gradient could explain milder OI symptoms observed for N-terminal glycine substitutions (e.g., almost no lethal substitutions in the N-ter-minal quarter of collagen were reported, and many of these cases were classified as type I OI). However, no consistent severity gradient and no correlations of symptoms with over-modification were found for mutations located further toward the C-terminal end. Thus, the role of overmodification in OI phenotype still remains unclear. 

Brasseur, G., Saribas, A. S., and Daldal F., 1996, A Compilation of mutations located in the Cytochrome b Subunit of the Bacterial and Mitochondrial bcl Complex, Biochim. Biophys. Acta 1275 61n69. 

The positions of the polymorphisms correspond to positions o MDR1 cDNA with the first base of die ATG start codon set to 1 (GenBank accession M14758). Mutations located in introns are given as position downstream (—) or upstream (+) of the respective exon according to file genomic organization ofMDRl as described by Chen et al. (105). 

In humans, hyperthyroidism, for example, can result from mutations located in the TSHR TM domains that activate the receptor. By contrast, thyroid adenomas and multinodular goiter [24-30] result from many somatic mutations affecting other regions of the TSHR. Such an example is a constitutively active TSHR mutation in the first TM domain that results from a Gly substitution at the conserved 431Ser position [27]. 

X- or gamma-rays Large deletions, several hundred kilobases in size Loss of function Easier to identify mutation location Can span several genes rearrangements are common... 

More than 700 mutations located throughout the gene have been identified in the CFTR gene in CF patients. The mutations include missense, nonsense, and frameshift mutations. In terms of functional defects, CFTR mutations have been grouped into four categories ... 

Kiachopoulos S, Bracher A, Winklhofer KF, Tatzelt J (2005) Pathogenic mutations located in the hydrophobic core of the prion protein interfere with folding and attachment of the glycosylphosphatidylinositol anchor. J Biol Chem 280 9320... 

Up to now pointmutations substituting amino-acid residues of the chromophore leading to altered spectral properties have only be described for Aequorea GFP. However, mutation located outside the chromophore can also change the spectra of fluorescent protein, indicating that the chromophore environment provided by the B-can structure of the protein is of equal importance, Fig. (5). 

To conclude this mutational pathway, PMIL was sculpted by 12 rounds of directed evolution, in which it accumulated 22 mutations (8 silent) throughout the entire fusion gene. Beneficial mutations that enhanced secretion or activity were located in the signal prepro-leader (5 mutations) and the mature protein (7 mutations), respectively. Significantly, only two mutations located in the second coordination sphere of the T1 copper site conferred tolerance to blood. Therefore, the re-specialization required to adapt the PMIL to such inclement conditions affected only 0.4% of the amino acid sequence. 

Mutations located in the C-terminal region of )3Gal can also be complemented in a manner similar to the mutations in the N-terminal region, and this is termed CO complementation. 

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